Margaret Robinson was first exposed about science early in her life from reading about Marie Curie. While enrolled at Smith College, she planned on being an English or theater major. However, due to university requirements, Margaret had to complete an introductory biology course. In that course, Jeanne Powell gave a lecture on cells and showed her students electron micrographs.[5] This is when Margaret really became interested in cellular biology; the complexity of cells intrigued her.

Robinson eventually joined a new lab and was able to conduct research on anything she liked. Due to her inexperience, her research did not go as planned and was nearly kicked out of graduate school.[5] Robinson had to stop working on her interest in coated vesicles and work on something closer to what the lab was researching.

Robinson eventually started a postdoctoral research with Barbara Pearse.[5] Her interest was in clathrin-coated vesicles that binds to cargo. She eventually succeeded in purifying components of the coat that were not clathrin and are now known as adaptor proteins.[5] These proteins sit between clathrin, which forms the vesicle’s outer shell and also the vesicle membrane. Continuing, Margaret discovered that there were two different populations of clathrin-coated vesicles, one that uses AP-2 at the plasma membrane and one that uses AP-1 and was associated with intracellular membranes.[5] AP-1 and AP-2 are both heterotetramers with related subunits. They both have two large subunits and the other subunit is closely related in AP-1 and AP-2.

Her achievements include the discovery of adaptins, which are specific proteins that manage cell-trafficking to ensure the correct cell cargo is transported to the right location.[2] She also discovered different combinations of adapting, when together with clathrin, form a coat around vesicles that bud from intracellular membranes and act as transporters for protein packages to be distributed in the cell. She also developed the technique “knock sideways,” which inactivates proteins in seconds.[7]

After finishing her postdoc, she was able to start her own lab. Her main focus was to learn more about the AP protein in depth.[5] She had to also work with DNA because in order to characterize the complexes thoroughly, she needed to clone the subunits. Robinson and her lab managed to find another AP complex, AP-3, which interacts with lysosomal membrane proteins such as LAMP1.[5]AP-3 also interacts with tyrosinase, which is a key enzyme in melanin biosynthesis, so AP-3 is important for tyrosinase trafficking to premelanosomes.[5]

Every form of eukaryotic life on earth contains coated vesicles and adaptors. Her work is also speculated to play a key role in evolution of eukaryotes form prokaryotes over two billion years ago. Her work also has medical implications. Some adaptors are mutated in certain genetic disorders, and adaptors are frequently exploited by pathogens . For example, the HIV genome encodes a protein called Nef, which is required for the development of AIDS, and which works by hijacking adaptors and using them to modify the surface of the infected cell.

Robinson’s work explains how coated vesicles sort cargo but also provides tools that can be used by others to address their own favorite problems. For instance, her newly developed method called knocksideways. Knocksideways gets rid of proteins rapidly. Her technique has found its way into other labs who are also interested in how particular proteins contribute to different stages of cell division.[8]